BMRB Entry 27753

Title:
The cytoplasm-entry domain of antibacterial CdiA is a dynamic alpha-helical bundle with disulfide-dependent structural features
Deposition date:
2019-01-15
Original release date:
2019-01-18
Authors:
Bartelli, Nicholas; Sun, Sheng; Gucinski, Grant; Zhou, Hongjun; Song, Kiho; Hayes, Christopher; Dahlquist, Frederick
Citation:

Citation: Bartelli, Nicholas; Sun, Sheng; Gucinski, Grant; Zhou, Hongjun; Song, Kiho; Hayes, Christopher; Dahlquist, Frederick. "The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic alpha-Helical Bundle with Disulfide-Dependent Structural Features"  J. Mol. Biol. 431, .-3203 (3216).
PubMed: 31181288

Assembly members:

Assembly members:
CdiA-CT, polymer, 150 residues, 15943 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21d

Data sets:
Data typeCount
13C chemical shifts421
15N chemical shifts136
1H chemical shifts847

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CdiA-CT1

Entities:

Entity 1, CdiA-CT 150 residues - 15943 Da.

1   VALGLUASNASNPHELEUTHRALAASPGLN
2   ILEASPSERPHEALAALALYSALALYSGLY
3   CYSGLUVALARGGLYASPCYSLYSGLNILE
4   VALLYSGLUMETGLUGLULEUSERLEULYS
5   GLNGLNGLNGLUMETILEALAVALCYSALA
6   THRASNPROALAALACYSLYSGLULYSPHE
7   GLYASPILEPROALALYSGLYMETLEUVAL
8   ARGGLUALAILEASPARGVALLEUGLYTHR
9   ASPVALPROSERALAMETLYSASNASPMET
10   SERSERLEULEUALAGLNGLNILEGLUALA
11   GLUGLYVALVALTHRSERTHRGLUPHEALA
12   SERGLNLEUGLNASNARGTYRGLYILEASP
13   LYSGLNGLNALAGLUILELEUALAVALALA
14   ALALEUGLYALAVALTHRGLYGLYMETGLY
15   LYSSERGLYTHRSERTHRVALTHRLYSASN

Samples:

sample_1: CdiA-CT, [U-99% 13C; U-99% 15N], 1.4 mM; sodium phosphate 50 mM; sodium azide 3 mM; Dithiothrietol 10 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

NCBI WP_001383049.1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks